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用氢-氘交换质谱法定义 Hsp33's 氧化还原调节陪护活动和 Hsp33 映射构象变化

JoVE Journal
Biochemistry

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JoVE Journal Biochemistry

Defining Hsp33’s Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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用氢-氘交换质谱法定义 Hsp33's 氧化还原调节陪护活动和 Hsp33 映射构象变化

DOI:

10.3791/57806-v

•

10:24 min

•

June 07, 2018

•

Rosi Fassler*¹, Nufar Edinger*¹, Oded Rimon, Dana Reichmann

¹Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram,The Hebrew University of Jerusalem

Chapters

00:04Title
00:44Preparation of Fully Reduced and Fully Oxidized Proteins
02:37Light Scattering Aggregation Assay
05:20Hydrogen-deuterium Exchange Mass Spectrometry (HDX-MS)
08:01Results: Investigation of Hsp33 s Redox-regulated Chaperone Activity and Structure Changes
09:34Conclusion

Summary

Automatic Translation

生物体在其一生中遇到的最具挑战性的压力条件之一是氧化剂的积累。在氧化应激过程中, 细胞大量依赖分子伴侣。在这里, 我们介绍了用于研究氧化还原调节的抗聚集活性的方法, 以及通过海达兴-MS 来监测调节陪护功能的结构变化。

Tags

Hsp33 Chaperone Activity Hydrogen-deuterium Exchange Mass Spectrometry Oxidative Stress Protein Aggregation Protein Dynamics Enzyme Interactions Visual Demonstration

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